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Gay, D.C., Spear, P.J., Keatinge-Clay, A.T. (2014). A double-hotdog with a new trick: structure and mechanism of the trans-acyltransferase polyketide synthase enoyl-isomerase. ACS Chem. Biol. 9:2374-81.
Garg, A., Xingiang, X., Keatinge-Clay, A.T., Khosla, C., Cane, D.E. (2014). Elucidation of the cryptic epimerase activity of redox-inactive ketoreductase domains from modular polyketide synthases by tandem equilibrium isotope exchange. J. Am. Chem. Soc. 136:10190-3.
Gay, D.C., Keatinge-Clay, A.T. (2014). Rapid modification of the pET-28 expression vector for ligation independent cloning using homologous recombination in Saccharomyces cerevisiae. Plasmid pii: S0147-619X(14)00075-4.
Fage, C.D., Henderson, J.C., Cannon, J.R., Brodbelt, J.S., Keatinge-Clay, A.T., Trent, M.S. (2014). Antimicrobial peptide resistance of Vibrio cholerae results from LPS modification pathway related to non-ribosomal peptide synthetases. ACS Chem. Biol. 9:2382-92.
Isiorho, E.A., Jeon, B.-S., Liu, H.-w., Keatinge-Clay, A.T. (2014) Structural studies of the spinosyn forosaminyltransferase, SpnP. Biochemistry 53:4292-301.
Fage, C.D., Brown, D.B., Boll, J.M., Keatinge-Clay, A.T., Trent, M.S. (2014). Crystallographic study of the EptC phosphoethanolamine transferase required for polymyxin resistance and motility in Campylobacter jejuni. Acta Cryst. D 70:2730-9.
Brantley, J.N., Bailey, C.B., Cannon, J.R., Clark, K.A., Vanden Bout, D.A., Brodbelt, J.S., Keatinge-Clay, A.T., Bielawski, C.W. (2014). Mechanically modulating the photophysical properties of fluorescent protein biocomposites: new classes of ratio- and intensiometric sensors. Angew. Chem. 53:5088-98.
Piasecki, S.K., Zheng, J., Axelrod, A.J., Detelich, M., Keatinge-Clay, A.T. (2014). Structural and functional studies of a trans-acyltransferase polyketide synthase ketoreductase the performs both alpha- and beta-ketoreduction. Proteins 82:2067-77.
Gay, D.C., Gay, G., Axelrod, A.J., Jenner, M., Kohlhaas, C., Kampa, A., Oldham, N.J., Piel, J., Keatinge-Clay, A.T. (2014). A close look at a ketosynthase from a trans-acyltransferase modular polyketide synthase. Structure 22:444-51.
Hughes, A.J., Tibby, M.R., Wagner, D.T., Brantley, J.N., Keatinge-Clay, A.T. (2014). Investigating the reactivities of a polyketide synthase module through fluorescent click chemistry. Chem. Commun. 50: 5276-8.
Gay, D.C., You, Y.-O., Keatinge-Clay, A.T., Cane D.E. (2013). Structural and stereospecificity of the dehydratase domain from the terminal module of the rifamycin polyketide synthase. Biochemistry 52:8916-28.
Enyeart, P.J., Chirieleison, S.M., Dao, M.N., Perutka, J., Quandt, E.M., Yao, J., Whitt, J.T., Keatinge-Clay, A.T., Lambowitz, A.M., Georgiou, G., Ellington, A.D. (2013). Generalized bacterial genome editing using mobile group II introns and Cre-lox. Mol. Syst. Biol. 9: 685-700.
Zheng, J., Piasecki, S.K., Keatinge-Clay, A.T. (2013). Structural studies of an A2-type modular polyketide synthase ketoreductase reveal features controlling alpha-substituent stereochemistry. ACS Chem. Biol. 8:1964-71.
Zheng, J., Fage, C.D., Demeler, B., Hoffman, D.W., Keatinge-Clay, A.T. (2013). The missing linker: a dimerization motif located within polyketide synthase modules. ACS Chem. Biol. 8:1263-70.
Brantley, J.N., Bailey, C.B., Wiggins, K.M., Keatinge-Clay, A.T., Bielawski, C.W. (2013). Mechanobiochemistry: harnessing biomacromolecules for force-responsive materials. Polym. Chem. 4:3916-28.
Zheng, J. & Keatinge-Clay, A.T. (2013). The status of type I polyketide synthase ketoreductases. Med. Chem. Commun. 4:34-40.
Harper, A.D., Bailey, C.B., Edwards, A.D., Detelich, J.F., Keatinge-Clay, A.T. (2012). Preparative, in vitro biocatalytic syntheses of triketide lactone building blocks. Chembiochem 13:2200-3.
Keatinge-Clay, A.T. (2012). The structures of type I polyketide synthases. Nat. Prod. Rep. 29:1050-73.
Piasecki, S.K. & Keatinge-Clay, A.T. (2012). Monitoring biocatalytic transformations mediated by polyketide synthase enzymes via fluorine NMR. Synlett 12:1840-2.
Zheng, J., Gay, D.C., Demeler, B., White, M.A., Keatinge-Clay, A.T. (2012). Divergence of multimodular polyketide synthases revealed by a didomain structure. Nat. Chem. Biol. 8:615-21.